1f99
From Proteopedia
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CRYSTAL STRUCTURE OF R-PHYCOCYANIN FROM POLYSIPHONIA AT 2.4 A RESOLUTION
Overview
The crystal structure of R-phycocyanin from Polysiphonia urceolata (R-PC-PU) at 2.4 A is reported. The R-PC-PU crystal belongs to space group P4(3)2(1)2 with cell parameters a = 135.1 A, c = 210.0 A, and alpha = beta = gamma = 90 degrees. The structure was determined by molecular replacement. The crystallographic R-factor of the refined model is 0.189 (R(free) = 0.239). Comparison of the microenvironment of chromophore beta 155 in R-PC-PU and in C-PC from Fremyolla diphosiphon (C-PC-FD) reveals that their spectral differences may be caused by their different alpha 28 residues. In the R-PC-PU crystal structure, two (alpha beta)(3) trimers assemble face to face to form a hexamer, and two such hexamers assemble in two novel side-to-side arrangements. Possible models for the energy transfer from phycoerythrin to phycocyanin and from phycocyanin to allophycocyanin are proposed based on several phycobiliprotein crystal structures.
About this Structure
1F99 is a Protein complex structure of sequences from Polysiphonia urceolata with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of R-phycocyanin and possible energy transfer pathways in the phycobilisome., Jiang T, Zhang JP, Chang WR, Liang DC, Biophys J. 2001 Aug;81(2):1171-9. PMID:11463658
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